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- PDB-7ovg: The C146A variant of an amidase from Pyrococcus horikoshii with b... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7ovg | ||||||
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Title | The C146A variant of an amidase from Pyrococcus horikoshii with bound acetamide | ||||||
![]() | CN hydrolase domain-containing protein | ||||||
![]() | HYDROLASE / Amidase / Nitrilase superfamily | ||||||
Function / homology | ![]() N-carbamoylputrescine amidase activity / beta-alanine biosynthetic process via 3-ureidopropionate / putrescine biosynthetic process from arginine / beta-ureidopropionase activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Su, S. / Makumire, S. / Sewell, B.T. | ||||||
Funding support | ![]()
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![]() | ![]() Title: The structures of the C146A variant of the amidase from Pyrococcus horikoshii bound to glutaramide and acetamide suggest the basis of amide recognition. Authors: Makumire, S. / Su, S. / Weber, B.W. / Woodward, J.D. / Wangari Kimani, S. / Hunter, R. / Sewell, B.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.2 KB | Display | ![]() |
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PDB format | ![]() | 92.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1005.5 KB | Display | ![]() |
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Full document | ![]() | 1005.3 KB | Display | |
Data in XML | ![]() | 21 KB | Display | |
Data in CIF | ![]() | 30.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ypaS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29950.490 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 Gene: PH0642 / Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.59 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop Details: The crystallization condition is: 5mg/mL protein, 0.1M potassium chloride, 0.2M Sodium formate; 0.2M Ammonium acetate; 0.2M Sodium citrate tribasic dihydrate; 0.2M Sodium potassium tartrate ...Details: The crystallization condition is: 5mg/mL protein, 0.1M potassium chloride, 0.2M Sodium formate; 0.2M Ammonium acetate; 0.2M Sodium citrate tribasic dihydrate; 0.2M Sodium potassium tartrate tetrahydrate; 0.1M acetamide; Imidazole; MES monohydrate (acid); 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350 |
-Data collection
Diffraction | Mean temperature: 170 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Sep 20, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→43.86 Å / Num. obs: 53852 / % possible obs: 81.14 % / Redundancy: 3.4 % / Biso Wilson estimate: 22.57 Å2 / CC1/2: 0.996 / CC star: 0.999 / Rmerge(I) obs: 0.056 / Rpim(I) all: 0.035 / Rrim(I) all: 0.065 / Net I/σ(I): 11.32 |
Reflection shell | Resolution: 1.65→1.709 Å / Redundancy: 3 % / Rmerge(I) obs: 0.3671 / Mean I/σ(I) obs: 2.39 / Num. unique obs: 2008 / CC1/2: 0.927 / CC star: 0.981 / Rpim(I) all: 0.2463 / Rrim(I) all: 0.4444 / % possible all: 30.28 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6YPA Resolution: 1.65→43.85 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.969 / SU B: 2.56 / SU ML: 0.078 / Cross valid method: THROUGHOUT / ESU R: 0.1 / ESU R Free: 0.097 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.3 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.106 Å2
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Refinement step | Cycle: LAST / Resolution: 1.65→43.85 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.65→1.693 Å / Total num. of bins used: 20
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